丁香假单胞菌丁香致病变种中藻酸盐裂解酶的特性分析
Characterization of alginate lyase from Pseudomonas syringae pv. syringae.
作者信息
Preston L A, Wong T Y, Bender C L, Schiller N L
机构信息
Division of Biomedical Sciences, University of California, Riverside, California 92521, USA.
出版信息
J Bacteriol. 2000 Nov;182(21):6268-71. doi: 10.1128/JB.182.21.6268-6271.2000.
Abstract
The gene encoding alginate lyase (algL) in Pseudomonas syringae pv. syringae was cloned, sequenced, and overexpressed in Escherichia coli. Alginate lyase activity was optimal when the pH was 7.0 and when assays were conducted at 42 degrees C in the presence of 0.2 M NaCl. In substrate specificity studies, AlgL from P. syringae showed a preference for deacetylated polymannuronic acid. Sequence alignment with other alginate lyases revealed conserved regions within AlgL likely to be important for the structure and/or function of the enzyme. Site-directed mutagenesis of histidine and tryptophan residues at positions 204 and 207, respectively, indicated that these amino acids are critical for lyase activity.
摘要
克隆、测序了丁香假单胞菌丁香致病变种中编码藻酸盐裂解酶（algL）的基因，并在大肠杆菌中进行了过表达。当pH值为7.0且在0.2 M NaCl存在下于42℃进行测定时，藻酸盐裂解酶活性最佳。在底物特异性研究中，来自丁香假单胞菌的AlgL对脱乙酰化的聚甘露糖醛酸表现出偏好。与其他藻酸盐裂解酶的序列比对揭示了AlgL内的保守区域，这些区域可能对该酶的结构和/或功能很重要。分别对位置204和207处的组氨酸和色氨酸残基进行定点诱变表明，这些氨基酸对裂解酶活性至关重要。
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